3VFA
Crystal Structure of HIV-1 Protease Mutant V82A with novel P1'-Ligands GRL-02031
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2008-07-09 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.644, 86.459, 45.441 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.430 |
| R-factor | 0.1703 |
| Rwork | 0.168 |
| R-free | 0.21810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h5b |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.029 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.480 |
| High resolution limit [Å] | 1.430 | 1.430 |
| Rmerge | 0.098 | 0.450 |
| Number of reflections | 39482 | |
| <I/σ(I)> | 12.1 | 2 |
| Completeness [%] | 90.5 | 57 |
| Redundancy | 4.5 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 298 | 0.6M NaCl, 0.1M Sodium Acetate buffer pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
